Nature Communications (May 2016)
Crystal structure of an invertebrate cytolysin pore reveals unique properties and mechanism of assembly
- Marjetka Podobnik,
- Peter Savory,
- Nejc Rojko,
- Matic Kisovec,
- Neil Wood,
- Richard Hambley,
- Jonathan Pugh,
- E. Jayne Wallace,
- Luke McNeill,
- Mark Bruce,
- Idlir Liko,
- Timothy M. Allison,
- Shahid Mehmood,
- Neval Yilmaz,
- Toshihide Kobayashi,
- Robert J. C. Gilbert,
- Carol V. Robinson,
- Lakmal Jayasinghe,
- Gregor Anderluh
Affiliations
- Marjetka Podobnik
- Department for Molecular Biology and Nanobiotechnology, National Institute of Chemistry
- Peter Savory
- Oxford Nanopore Technologies Ltd., Edmund Cartwright House, 4 Robert Robinson Avenue, Oxford Science Park
- Nejc Rojko
- Department for Molecular Biology and Nanobiotechnology, National Institute of Chemistry
- Matic Kisovec
- Department for Molecular Biology and Nanobiotechnology, National Institute of Chemistry
- Neil Wood
- Oxford Nanopore Technologies Ltd., Edmund Cartwright House, 4 Robert Robinson Avenue, Oxford Science Park
- Richard Hambley
- Oxford Nanopore Technologies Ltd., Edmund Cartwright House, 4 Robert Robinson Avenue, Oxford Science Park
- Jonathan Pugh
- Oxford Nanopore Technologies Ltd., Edmund Cartwright House, 4 Robert Robinson Avenue, Oxford Science Park
- E. Jayne Wallace
- Oxford Nanopore Technologies Ltd., Edmund Cartwright House, 4 Robert Robinson Avenue, Oxford Science Park
- Luke McNeill
- Oxford Nanopore Technologies Ltd., Edmund Cartwright House, 4 Robert Robinson Avenue, Oxford Science Park
- Mark Bruce
- Oxford Nanopore Technologies Ltd., Edmund Cartwright House, 4 Robert Robinson Avenue, Oxford Science Park
- Idlir Liko
- Department of Chemistry, University of Oxford
- Timothy M. Allison
- Department of Chemistry, University of Oxford
- Shahid Mehmood
- Department of Chemistry, University of Oxford
- Neval Yilmaz
- Lipid Biology Laboratory, RIKEN Institute
- Toshihide Kobayashi
- Lipid Biology Laboratory, RIKEN Institute
- Robert J. C. Gilbert
- Division of Structural Biology, Wellcome Trust Centre for Human Genetics, University of Oxford
- Carol V. Robinson
- Department of Chemistry, University of Oxford
- Lakmal Jayasinghe
- Oxford Nanopore Technologies Ltd., Edmund Cartwright House, 4 Robert Robinson Avenue, Oxford Science Park
- Gregor Anderluh
- Department for Molecular Biology and Nanobiotechnology, National Institute of Chemistry
- DOI
- https://doi.org/10.1038/ncomms11598
- Journal volume & issue
-
Vol. 7,
no. 1
pp. 1 – 10
Abstract
Pore-forming toxins act by forming oligomeric pores in lipid membranes. Here the authors report the crystal structure of the lysenin pore, providing insights into the assembly and function of the pore in addition to suggesting that its properties make lysenin potentially well-suited for nanopore sensing applications.
